Spectrin/band 3 ratio as diagnostic tool in hereditary spherocytosis

1992 ◽  
Vol 151 (1) ◽  
pp. 35-37
Author(s):  
S. Cutillo ◽  
L. Pinto ◽  
B. Nobili ◽  
E. Miraglia del Giudice ◽  
A. Iolascon
Keyword(s):  
Diagnostic Tool ◽  
Hereditary Spherocytosis ◽  
Band 3

scholarly journals Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III

2001 ◽  
Vol 113 (3) ◽  
pp. 689-693 ◽  
Author(s):  
Natalie A. Bracher ◽  
Cheryl A. Lyons ◽  
Glynn Wessels ◽  
Erna Mansvelt ◽  
Thérèsa L. Coetzer
Keyword(s):  
Hereditary Spherocytosis ◽  
Cape Town ◽  
Band 3

scholarly journals Modulation of Clinical Expression and Band 3 Deficiency in Hereditary Spherocytosis

Blood ◽  
1997 ◽  
Vol 90 (1) ◽  
pp. 414-420 ◽  
Author(s):  
N. Alloisio ◽  
P. Texier ◽  
A. Vallier ◽  
M.L. Ribeiro ◽  
L. Morlé ◽  
...  
Keyword(s):  
Binding Sites ◽  
Hereditary Spherocytosis ◽  
Novel Mutation ◽  
Band 3 ◽  
Anion Exchanger 1 ◽  
Severe Clinical Picture ◽  
In Trans ◽  
Novel Alleles ◽  
Pronounced Reduction ◽  
Compound Heterozygotes

Abstract We present two novel alleles of the anion-exchanger 1 (AE1) gene, allele Coimbra and allele Mondego. Allele Coimbra (V488M, GTG → ATG) affects a conserved position in the putative second ectoplasmic loop of erythrocyte band 3. In 15 simple heterozygotes, it yielded a mild form of hereditary spherocytosis (HS) with band 3 deficiency (−20% ± 2%) and a reduced number of 4,4′-diisothiocyano-1,2-diphenylethane-2,2′-disulfonate (H2DIDS) binding sites (−35%). However, two additional heterozygotes presented with an aggravated HS and a more pronounced reduction of band 3 (−40%) and of H2DIDS binding sites (−48%). They carried, in trans to allele Coimbra, allele Mondego, defined by two mutations: E40K, GAG → AAG, the known mutation Montefiore, and P147S, CCT → TCT, a novel mutation, both located in the cytoplasmic domain of band 3. Allele Mondego itself resulted in no clinical or hematologic HS signs in the simple heterozygous state. Yet it yielded a slight decrease in band 3 (−6% to −12%) and in the number of H2DIDS binding sites (−19%). Thus, the more pronounced decrease in band 3 in the two compound heterozygotes derived from the additive effects of two unequally expressed AE1 alleles, resulting in a more severe clinical picture.

scholarly journals Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis

Blood ◽  
1993 ◽  
Vol 82 (10) ◽  
pp. 2953-2960 ◽  
Author(s):  
P Savvides ◽  
O Shalev ◽  
KM John ◽  
SE Lux
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Autosomal Dominant ◽  
Hereditary Spherocytosis ◽  
Band 3 ◽  
Normal Range ◽  
Dominant Form ◽  
Autosomal Dominant Form ◽  
The Common ◽  
Ankyrin Deficiency

Abstract The common autosomal dominant form of hereditary spherocytosis (HS) has been genetically linked to defects of the erythroid ankyrin gene in a few families; however, the frequency of ankyrin deficiency and its relationship to red blood cell (RBC) spectrin content are unknown. To test these questions, we measured RBC spectrin and ankyrin by radioimmunoassay in 39 patients from 20 families with dominant HS. Normal RBCs contained 242,000 +/- 20,500 spectrin heterodimers and 124,500 +/- 11,000 ankyrins per cell. In dominant HS, RBC spectrin and ankyrin ranged from about 40% to 100% of normal and were continuously distributed. Measurements in the same patient on different occasions were reproducible (+/- 5% to 10%) and RBCs from affected members of a kindred contained similar amounts of spectrin and ankyrin (+/- 3% to 4%). Spectrin and ankyrin levels were almost always less than the assay controls, but were less than the normal range in only 75% and 80% of kindreds, respectively. Remarkably, the degree of RBC spectrin and ankyrin deficiency was very similar in 19 of 20 HS kindreds. One otherwise typical family differed, with marked ankyrin deficiency (45% of control) and a relatively mild spectrin deficit (81%). We conclude that most patients with dominant HS have combined ankyrin and spectrin deficiency and that the two proteins are usually about equally deficient, suggesting that defects in ankyrin expression, ankyrin stability, or ankyrin band 3 (AE1) interactions may be common in dominant HS.

scholarly journals Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4366-4374 ◽  
Author(s):  
P Jarolim ◽  
JL Murray ◽  
HL Rubin ◽  
WM Taylor ◽  
JT Prchal ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Autosomal Dominant ◽  
Hereditary Spherocytosis ◽  
Gene Mutations ◽  
Band 3 ◽  
Red Cell Membrane ◽  
Cell Membrane Proteins ◽  
Gene Defects ◽  
Relative Deficiency ◽  
Peripheral Blood Smears

Abstract Hereditary spherocytosis (HS) is a common hemolytic anemia of variable clinical expression. Pathogenesis of HS has been associated with defects of several red cell membrane proteins including erythroid band 3. We have studied erythrocyte membrane proteins in 166 families with autosomal dominant HS. We have detected relative deficiency of band 3 in 38 kindred (23%). Band 3 deficiency was invariably associated with mild autosomal dominant spherocytosis and with the presence of pincered red cells in the peripheral blood smears of unsplenectomized patients. We hypothesized that this phenotype is caused by band 3 gene defects. Therefore, we screened band 3 DNA from these 38 kindred for single strand conformational polymorphisms (SSCP). In addition to five mutations detected previously by SSCP screening of cDNA, we detected 13 new band 3 gene mutations in 14 kindred coinherited with HS. These novel mutations consisted of two distinct subsets. The first subset included seven nonsense and frameshift mutations that were all associated with the absence of the mutant mRNA allele from reticulocyte RNA, implicating decreased production and/or stability of mutant mRNA as the cause of decreased band 3 synthesis. The second group included five substitutions of highly conserved amino acids and one in-frame deletion. These six mutations were associated with the presence of comparable levels of normal and mutant band 3 mRNA. We suggest that these mutations interfere with band 3 biosynthesis leading thus to the decreased accumulation of the mutant band 3 allele in the plasma membrane.

Flow Cytometry as a Diagnostic Tool for Hereditary Spherocytosis

2006 ◽  
Vol 116 (3) ◽  
pp. 186-191 ◽  
Author(s):  
Gudrun Stoya ◽  
Bernd Gruhn ◽  
Heinz Vogelsang ◽  
Eckehard Baumann ◽  
Werner Linss
Keyword(s):  
Flow Cytometry ◽  
Diagnostic Tool ◽  
Hereditary Spherocytosis

scholarly journals Cryohemolysis test as a diagnostic tool for hereditary spherocytosis

1999 ◽  
Vol 78 (12) ◽  
pp. 555-557 ◽  
Author(s):  
A. Iglauer ◽  
D. Reinhardt ◽  
W. Schröter ◽  
A. Pekrun
Keyword(s):  
Diagnostic Tool ◽  
Hereditary Spherocytosis

scholarly journals Modulation of Clinical Expression and Band 3 Deficiency in Hereditary Spherocytosis

Blood ◽  
1997 ◽  
Vol 90 (1) ◽  
pp. 414-420 ◽  
Author(s):  
N. Alloisio ◽  
P. Texier ◽  
A. Vallier ◽  
M.L. Ribeiro ◽  
L. Morlé ◽  
...  
Keyword(s):  
Binding Sites ◽  
Hereditary Spherocytosis ◽  
Novel Mutation ◽  
Band 3 ◽  
Anion Exchanger 1 ◽  
Severe Clinical Picture ◽  
In Trans ◽  
Novel Alleles ◽  
Pronounced Reduction ◽  
Compound Heterozygotes

We present two novel alleles of the anion-exchanger 1 (AE1) gene, allele Coimbra and allele Mondego. Allele Coimbra (V488M, GTG → ATG) affects a conserved position in the putative second ectoplasmic loop of erythrocyte band 3. In 15 simple heterozygotes, it yielded a mild form of hereditary spherocytosis (HS) with band 3 deficiency (−20% ± 2%) and a reduced number of 4,4′-diisothiocyano-1,2-diphenylethane-2,2′-disulfonate (H2DIDS) binding sites (−35%). However, two additional heterozygotes presented with an aggravated HS and a more pronounced reduction of band 3 (−40%) and of H2DIDS binding sites (−48%). They carried, in trans to allele Coimbra, allele Mondego, defined by two mutations: E40K, GAG → AAG, the known mutation Montefiore, and P147S, CCT → TCT, a novel mutation, both located in the cytoplasmic domain of band 3. Allele Mondego itself resulted in no clinical or hematologic HS signs in the simple heterozygous state. Yet it yielded a slight decrease in band 3 (−6% to −12%) and in the number of H2DIDS binding sites (−19%). Thus, the more pronounced decrease in band 3 in the two compound heterozygotes derived from the additive effects of two unequally expressed AE1 alleles, resulting in a more severe clinical picture.

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